Isolation, Purification and Characterization of Phytase from Asperfillus sp.

Aspergillus속 균주가 생산하는 Phytase의 분리 정제 및 특성

  • 천성숙 (영남대학교 식품가공학과) ;
  • 조영제 (상주산업대학교 식품공학과) ;
  • 차원섭 (상주산업대학교 식품공학과) ;
  • 이희덕 (영남대학교 식품가공학과) ;
  • 이선호 (영남대학교 식품가공학과)
  • Published : 1998.02.01

Abstract

To extract insoluble proteins and to improve funtional properties of abolished proteins, an phytase producing Aspergillus sp. SM-15 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. Phytase production reached to maximum when the wheat bran medium containing 1% mannose, 1% yeast extract, 1% (NH4)2HPO4 and 0.2% calcium chloride was cultured for 4 days. Phytase was purified 17.1 fold and specific activity was 244.32unit/mg by a sequencial process of ammonium sulfate fraction, ion exchange chromatography and gel filtrations Pruified enzyme was confirmed as a single band by the polyacrylamide gel electro-phoresis. The molecular weight of phytase was estimated to be 46,000. The optimum pH and temperature for the phytase activity were 5.5 and 5$0^{\circ}C$. The enzyme is stable in pH 4.5~5.5, 6$0^{\circ}C$. The activity of purified enzyme was inhibited by Hg2+ whereas activited by Pb2+ and Fe2+. The activity of phytase was inhibited by the treatment with iodine. The result indicate the possible involvement of histidine at active site. Km and Vmax of the puridied phytase were 37.037mM/L and 159.87umol/min, respectively.

Keywords

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